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Archives of Biochemistry and Biophysics

Volumn 490, Issue 2, 2009, Pages 158-162

A residue-level investigation of the equilibrium unfolding of the C2A domain of synaptotagmin 1

(4) Anbazhagan, Veerappan a Wang, Han Min a Lu, Ching Song b Yu, Chin a

a NATIONAL TSING HUA UNIVERSITY (Taiwan)

b CHANG GUNG UNIVERSITY (Taiwan)

Author keywords

C2A domain; Equilibrium unfolding; NMR; Residue level; Urea

Indexed keywords

FIBROBLAST GROWTH FACTOR 1; PROTEIN S 100; SYNAPTOTAGMIN I; UREA;

ANIMAL CELL; ARTICLE; CELL STRESS; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; HETERONUCLEAR SINGLE QUANTUM COHERENCE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN STRUCTURE; RAT; STEADY STATE; THERMODYNAMICS;

ANIMALS; FIBROBLAST GROWTH FACTOR 1; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RATS; RECOMBINANT PROTEINS; SYNAPTOTAGMIN I; THERMODYNAMICS; UREA;

EID: 70349751943 PISSN: 00039861 EISSN: 10960384 Source Type: Journal
DOI: 10.1016/j.abb.2009.08.018 Document Type: Article

Times cited : (1)

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